Remarkable stability of the proton translocating F1FO-ATP synthase from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1

Biochimica Et Biophysica Acta
Tina SuhaiH Seelert

Abstract

For functional characterization, we isolated the F1FO-ATP synthase of the thermophilic cyanobacterium Thermosynechococcus elongatus. Because of the high content of phycobilisomes, a combination of dye-ligand chromatography and anion exchange chromatography was necessary to yield highly pure ATP synthase. All nine single F1FO subunits were identified by mass spectrometry. Western blotting revealed the SDS stable oligomer of subunits c in T. elongatus. In contrast to the mass archived in the database (10,141 Da), MALDI-TOF-MS revealed a mass of the subunit c monomer of only 8238 Da. A notable feature of the ATP synthase was its ability to synthesize ATP in a wide temperature range and its stability against chaotropic reagents. After reconstitution of F1FO into liposomes, ATP synthesis energized by an applied electrochemical proton gradient demonstrated functional integrity. The highest ATP synthesis rate was determined at the natural growth temperature of 55 degrees C, but even at 95 degrees C ATP production occurred. In contrast to other prokaryotic and eukaryotic ATP synthases which can be disassembled with Coomassie dye into the membrane integral and the hydrophilic part, the F1FO-ATP synthase possessed a particular stability....Continue Reading

References

Dec 15, 1975·Biochemical and Biophysical Research Communications·M YoshidaY Kagawa
Nov 2, 1979·Biochimica Et Biophysica Acta·C W Campbell
Oct 29, 1987·Biochimica Et Biophysica Acta·M TomitaT Y Tsong
May 9, 1972·Biochemistry·K H Dooley, F J Castellino
Jun 1, 1982·Analytical Biochemistry·D Freifelder, M Better
Oct 1, 1994·European Journal of Biochemistry·S FischerP Gräber
Mar 8, 1994·Biochimica Et Biophysica Acta·H LillN Nelson
Mar 1, 1996·Analytical Chemistry·A ShevchenkoM Mann
Jul 1, 1997·Journal of Structural Biology·D NeffN A Dencher
Jan 23, 1999·Current Opinion in Structural Biology·R Jaenicke, G Böhm
Nov 24, 1999·Biochemical and Biophysical Research Communications·A PoetschN A Dencher
Nov 27, 1999·Science·D StockJ E Walker
Jun 6, 2000·Nature·H SeelertD J Müller
Mar 21, 2001·Critical Reviews in Biochemistry and Molecular Biology·R Sterner, W Liebl
Mar 27, 2001·EMBO Reports·H StahlbergP Dimroth
Apr 26, 2001·Proceedings of the National Academy of Sciences of the United States of America·W JiangR H Fillingame
Sep 21, 2002·DNA Research : an International Journal for Rapid Publication of Reports on Genes and Genomes·Yasukazu NakamuraSatoshi Tabata
Dec 19, 2002·Journal of Molecular Biology·Thomas MeierPeter Dimroth
Oct 8, 2003·Journal of Molecular Biology·Holger SeelertDaniel J Müller
Jan 9, 2004·Nature·A BekkerN J Beukes
Aug 11, 2004·Proceedings of the National Academy of Sciences of the United States of America·Noriyo MitomeMasasuke Yoshida
Oct 30, 2004·Biochimica Et Biophysica Acta·Jürgen M W Meyer Zu TittingdorfHolger Seelert
Feb 18, 2005·Proteomics·Daniela SchluesenerAnsgar Poetsch
Aug 23, 2006·Proceedings of the National Academy of Sciences of the United States of America·Armen Y MulkidjanianMichael Y Galperin
Jun 5, 2007·Journal of Bacteriology·Denys PogoryelovThomas Meier

❮ Previous
Next ❯

Citations

Sep 29, 2009·Electrophoresis·Tina SuhaiHolger Seelert
Jun 18, 2011·Biochimica Et Biophysica Acta·Holger Seelert, Norbert A Dencher
Apr 1, 2014·Bioscience Reports·Asha Manikkoth BalakrishnaGerhard Grüber
Dec 8, 2019·Scientific Reports·A V VlasovV I Gordeliy

❮ Previous
Next ❯

Related Concepts

Related Feeds

ATP Synthases

ATP synthases are enzymes located in the inner mitochondrial membrane that catalyze the synthesis of ATP during cellular respiration. Discover the latest research on ATP synthases here.